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Site‐specific N‐glycosylation regulates the GPS auto‐proteolysis of CD97
Author(s) -
Hsiao Cheng-Chih,
Cheng Kai-Fong,
Chen Hsin-Yi,
Chou Yi-Hua,
Stacey Martin,
Chang Gin-Wen,
Lin Hsi-Hsien
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.09.001
Subject(s) - proteolysis , glycosylation , g protein coupled receptor , receptor , chemistry , biochemistry , microbiology and biotechnology , biology , enzyme
Auto‐proteolysis at the G protein‐coupled receptor (GPCR) proteolytic site (GPS) is a hallmark of adhesion‐GPCRs. Although defects in GPS auto‐proteolysis have been linked to genetic disorders, information on its regulation remains elusive. Here, we investigated the GPS proteolysis of CD97, a human leukocyte‐restricted and tumor‐associated adhesion‐GPCR. We found that CD97 is incompletely processed, unlike its close homolog, epidermal growth factor‐like module‐containing mucin‐like hormone receptor 2. A unique pattern of N‐glycosylation within the GPS motif of related adhesion‐GPCRs was identified. The use of N‐glycosylation inhibitors and mutants confirm site‐specific N‐glycosylation is an important determinant of GPS proteolysis in CD97. Our results suggest that N‐glycosylation may regulate the processing of adhesion‐GPCRs leading to the production of either cleaved or uncleaved molecules.